Analytical Data
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Gene name
GAL3ST1
- Application
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Alternative Names
GAL3ST1；CST；Galactosylceramide sulfotransferase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99999
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Expression Region
1-423aa
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AA Sequence
MLPPQKKPWESMAKGLVLGALFTSFLLLVYSYAVPPLHAGLASTTPEAAASCSPPALEPEAVIRANGSAGECQPRRNIVFLKTHKTASSTLLNILFRFGQKHRLKFAFPNGRNDFDYPTFFARSLVQDYRPGACFNIICNHMRFHYDEVRGLVPTNAIFITVLRDPARLFESSFHYFGPVVPLTWKLSAGDKLTEFLQDPDRYYDPNGFNAHYLRNLLFFDLGYDNSLDPSSPQVQEHILEVERRFHLVLLQEYFDESLVLLKDLLCWELEDVLYFKLNARRDSPVPRLSGELYGRATAWNMLDSHLYRHFNASFWRKVEAFGRERMAREVAALRHANERMRTICIDGGHAVDAAAIQDEAMQPWQPLGTKSILGYNLKKSIGQRHAQLCRRMLTPEIQYLMDLGANLWVTKLWKFIRDFLRW
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
GAL3ST1, or Galactose-3-O-sulfotransferase 1, is an enzyme critical for the synthesis of sulfated glycosaminoglycans, particularly heparan sulfate, which plays essential roles in various biological processes, including cell signaling, regulation of growth factors, and modulation of blood coagulation. Abnormal expression or function of GAL3ST1 has been implicated in several pathologies, including cancer metastasis and developmental disorders. As such, understanding the structure and function of this enzyme is pivotal for both basic and applied research. Recent studies have focused on characterizing recombinant GAL3ST1 proteins to elucidate their biochemical properties and interactions with substrates, providing insights into its catalytic mechanisms. Techniques such as site-directed mutagenesis, crystallography, and enzymatic assays are employed to study the enzyme's activity and specificity. The production of GAL3ST1 as a recombinant protein not only aids in dissecting its functional roles in physiological and pathological contexts but also opens avenues for therapeutic interventions by developing inhibitors or substrates that target its activity. The findings from these studies may reveal novel strategies for treating diseases linked to glycosaminoglycan dysregulation and enhance our understanding of glycosylation processes in cell biology.
